Calcyclin-Like Protein from Ehrlich Ascites Tumour Cells - Ca2+ -Binding Properties, Distribution and Target Protein
We have purified to homogeneity a 10.5 kDa Ca2+-binding protein from Ehrlich ascites tumour (EAT) cells (Kuznicki & Filipek, 1987). This protein differs from S-100 protein, calbindin 9k, parvalbumin and on comodulin by several criteria such as electrophoretic mobility in SDS- or urea-polyacrylamide gels, amino acid composition, and lack of cross-reactivity with the antibodies specific to these Ca2+-binding proteins. Recently, we found that the partial amino acid sequence of the 10.5 kDa Ca2+- binding protein from EAT cells is homologous to that of human calcyclin, and therefore we call the mouse protein a calcydin-like protein (Kuznicki et al., 1989a). Calcyclin is the name given to the growth factor-inducible gene (Calabretta et al., 1986a; 1986b). It has been suggested that calcyclin protein is involved in the control of cell proliferation and may bind Ca2+, as deduced from nucleotide sequence of the gene. To our best knowledge nobody has so far studied the protein itself.
KeywordsZinc Filtration Urea Tyrosine Titration
Unable to display preview. Download preview PDF.
- Filipek, A., Heizmann, C. W., and Kunicki, J., Zinc binding and dimer formation by calcyclin-like calcium binding protein from Ehrlich ascites tumour cells, in: “Proceedings of First European Symposium on Calcium Binding Proteins in Normal and Transformed Cells”, R. Pochet, D.E.M. Lawson and C.W. Heizmann, eds., Plenum Press (1989)Google Scholar
- Kunicki, J., and Filipek, A., 1987, Purification and properties of a novel Ca2+-binding protein (10.5 kDa) from Ehrlich-ascites-tumour cells. Biochem. J., 247: 663.Google Scholar
- Kunicki, J., Filipek, A., Hunziker, P. E., Huber, S., and Heizmann, C. W., 1989a, Calcium binding protein from mouse Ehrlich ascites tumour cells is homologous to human calcyclin. Biochem. J., in press.Google Scholar
- Kunicki, J., Filipek, A., Heimann, P., Kaczmarek, L., Kaminska, B., 1989b, Tissue specific distribution of the calcyclin-like 10.5 kDa calcium binding protein. FEBS Lett., in press.Google Scholar